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rdf:type |
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lifeskim:mentions |
umls-concept:C0016055,
umls-concept:C0021701,
umls-concept:C0040690,
umls-concept:C0205275,
umls-concept:C0332256,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704241,
umls-concept:C1879547
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pubmed:issue |
13
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pubmed:dateCreated |
2005-11-1
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pubmed:abstractText |
Transforming growth factor-betas (TGF-beta) are secreted as latent complexes consisting of the TGF-beta dimer, the TGF-beta propeptide dimer, and the latent TGF-beta binding protein (LTBP). Although the bonds between TGF-beta and its propeptide are cleaved intracellulary, the propeptide associates with TGF-beta by electrostatic interactions, thereby conferring latency to the complex. We reported that a specific sequence of LTBP-1 is required for latent TGF-beta activation by the integrin alphavbeta6. Here we describe a 24 amino acid sequence from the hinge domain required for activation. The LTBP-1 polypeptide rL1N, which includes the hinge, associates with fibronectin in binding assays. We present evidence that fibronectin null cells minimally activate latent TGF-beta and poorly incorporate the active hinge sequence into their matrix. In addition, cells missing the fibronectin receptor alpha5beta1 exhibit defective activation of latent TGF-beta by alphavbeta6 and decreased matrix incorporation. The results indicate specificity for integrin-mediated latent TGF-beta activation that include unique sequences in LTBP-1 and an appropriate matrix molecule.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Collodion,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Latent TGF-beta Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ltbp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/integrin alphavbeta6
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1530-6860
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1798-808
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16260650-Amino Acid Sequence,
pubmed-meshheading:16260650-Animals,
pubmed-meshheading:16260650-Antigens, Neoplasm,
pubmed-meshheading:16260650-Biological Assay,
pubmed-meshheading:16260650-Blotting, Western,
pubmed-meshheading:16260650-CHO Cells,
pubmed-meshheading:16260650-Collodion,
pubmed-meshheading:16260650-Cricetinae,
pubmed-meshheading:16260650-Dimerization,
pubmed-meshheading:16260650-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:16260650-Epitopes,
pubmed-meshheading:16260650-Fibronectins,
pubmed-meshheading:16260650-Genetic Vectors,
pubmed-meshheading:16260650-Integrins,
pubmed-meshheading:16260650-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:16260650-Latent TGF-beta Binding Proteins,
pubmed-meshheading:16260650-Luciferases,
pubmed-meshheading:16260650-Mice,
pubmed-meshheading:16260650-Microscopy, Fluorescence,
pubmed-meshheading:16260650-Molecular Sequence Data,
pubmed-meshheading:16260650-Peptides,
pubmed-meshheading:16260650-Protein Binding,
pubmed-meshheading:16260650-Protein Structure, Tertiary,
pubmed-meshheading:16260650-RNA, Messenger,
pubmed-meshheading:16260650-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:16260650-Time Factors,
pubmed-meshheading:16260650-Transforming Growth Factor beta
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pubmed:year |
2005
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pubmed:articleTitle |
Fibronectin is required for integrin alphavbeta6-mediated activation of latent TGF-beta complexes containing LTBP-1.
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pubmed:affiliation |
Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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